HEADER TRANSFERASE 03-JUN-07 2Q5W
TITLE THE X-RAY CRYSTAL STRUCTURE OF MOLYBDOPTERIN SYNTHASE FROM
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN-CONVERTING FACTOR SUBUNIT 2;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: MPT SYNTHASE SUBUNIT 2, MOLYBDOPTERIN SYNTHASE SUBUNIT 2,
COMPND 5 MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN E, MOLYBDOPTERIN-CONVERTING
COMPND 6 FACTOR LARGE SUBUNIT;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1;
COMPND 10 CHAIN: D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: MOAE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 12 ORGANISM_TAXID: 1280;
SOURCE 13 GENE: MOAD;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS MOLYBDOPTERIN, MOCO, MPT SYNTHASE, MOAD, MOAE, TRANSFERASE,
KEYWDS 2 MOLYBDENUM COFACTOR BIOSYNTHESIS, BETA-GRASP (UBIQUITIN-LIKE), ALPHA
KEYWDS 3 BETA HAMMERHEAD FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR J.N.DANIELS,H.SCHINDELIN
REVDAT 5 30-AUG-23 2Q5W 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2Q5W 1 REMARK
REVDAT 3 13-JUL-11 2Q5W 1 VERSN
REVDAT 2 24-FEB-09 2Q5W 1 VERSN
REVDAT 1 19-FEB-08 2Q5W 0
JRNL AUTH J.N.DANIELS,M.M.WUEBBENS,K.V.RAJAGOPALAN,H.SCHINDELIN
JRNL TITL CRYSTAL STRUCTURE OF A MOLYBDOPTERIN SYNTHASE-PRECURSOR Z
JRNL TITL 2 COMPLEX: INSIGHT INTO ITS SULFUR TRANSFER MECHANISM AND ITS
JRNL TITL 3 ROLE IN MOLYBDENUM COFACTOR DEFICIENCY.
JRNL REF BIOCHEMISTRY V. 47 615 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18092812
JRNL DOI 10.1021/BI701734G
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 15548
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 824
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 821
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.1540
REMARK 3 BIN FREE R VALUE SET COUNT : 36
REMARK 3 BIN FREE R VALUE : 0.2120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1761
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.02000
REMARK 3 B22 (A**2) : 2.02000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.848
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1807 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1634 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2447 ; 1.551 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3823 ; 0.830 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 212 ; 6.771 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;37.473 ;25.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 326 ;13.586 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;22.417 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1972 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 346 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 304 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1624 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 883 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1045 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 112 ; 0.185 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.262 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.192 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.275 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1395 ; 1.162 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 432 ; 0.252 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1745 ; 1.308 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 877 ; 2.598 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 702 ; 3.638 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 21
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4400 11.0840 12.2380
REMARK 3 T TENSOR
REMARK 3 T11: -0.1253 T22: -0.1408
REMARK 3 T33: -0.0221 T12: 0.0104
REMARK 3 T13: -0.0571 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 5.3867 L22: 7.4351
REMARK 3 L33: 9.6306 L12: 0.8816
REMARK 3 L13: -0.6450 L23: -0.4470
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: 0.3495 S13: 0.3834
REMARK 3 S21: -0.2342 S22: 0.1744 S23: 0.6621
REMARK 3 S31: -0.4000 S32: -0.4506 S33: -0.2450
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 22 D 41
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4930 2.1280 14.7420
REMARK 3 T TENSOR
REMARK 3 T11: -0.1349 T22: -0.1425
REMARK 3 T33: 0.1307 T12: 0.0161
REMARK 3 T13: -0.0032 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 3.9554 L22: 4.6134
REMARK 3 L33: 14.5823 L12: 4.0108
REMARK 3 L13: -1.5580 L23: -3.9819
REMARK 3 S TENSOR
REMARK 3 S11: 0.1817 S12: 0.2950 S13: 0.5022
REMARK 3 S21: -0.0515 S22: 0.1554 S23: 1.0432
REMARK 3 S31: -0.5568 S32: -0.3690 S33: -0.3371
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 42 D 48
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8390 -1.0090 8.7670
REMARK 3 T TENSOR
REMARK 3 T11: -0.0207 T22: -0.0818
REMARK 3 T33: 0.0124 T12: -0.0322
REMARK 3 T13: -0.0276 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 11.4313 L22: 11.3436
REMARK 3 L33: 29.7134 L12: -6.6578
REMARK 3 L13: 7.6580 L23: -1.2642
REMARK 3 S TENSOR
REMARK 3 S11: 0.5179 S12: 0.9909 S13: -1.1373
REMARK 3 S21: -0.7955 S22: -0.1550 S23: 0.4948
REMARK 3 S31: 1.3407 S32: 0.4661 S33: -0.3629
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 49 D 55
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1240 3.5090 24.0790
REMARK 3 T TENSOR
REMARK 3 T11: -0.0851 T22: -0.1770
REMARK 3 T33: -0.0956 T12: -0.0136
REMARK 3 T13: 0.0035 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 3.7575 L22: 12.5188
REMARK 3 L33: 5.6994 L12: 0.7660
REMARK 3 L13: -3.9456 L23: 1.7861
REMARK 3 S TENSOR
REMARK 3 S11: 0.2080 S12: -0.4267 S13: 0.1303
REMARK 3 S21: 0.6953 S22: 0.0785 S23: -0.2448
REMARK 3 S31: 0.0807 S32: 0.3100 S33: -0.2865
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 56 D 77
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0810 2.2550 20.7080
REMARK 3 T TENSOR
REMARK 3 T11: -0.1233 T22: -0.1765
REMARK 3 T33: -0.0880 T12: 0.0037
REMARK 3 T13: 0.0039 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 3.5959 L22: 2.9117
REMARK 3 L33: 3.1691 L12: 3.1979
REMARK 3 L13: -2.0125 L23: -1.4624
REMARK 3 S TENSOR
REMARK 3 S11: 0.2066 S12: -0.0778 S13: 0.2339
REMARK 3 S21: 0.2229 S22: 0.0052 S23: 0.3302
REMARK 3 S31: 0.0092 S32: -0.0321 S33: -0.2118
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 37
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8650 12.9620 24.4590
REMARK 3 T TENSOR
REMARK 3 T11: -0.1284 T22: -0.1239
REMARK 3 T33: -0.1222 T12: -0.0465
REMARK 3 T13: -0.0057 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 3.1790 L22: 0.5572
REMARK 3 L33: 2.8619 L12: -1.2161
REMARK 3 L13: 1.4702 L23: -0.9078
REMARK 3 S TENSOR
REMARK 3 S11: -0.1412 S12: -0.0530 S13: 0.4179
REMARK 3 S21: 0.0998 S22: -0.0055 S23: -0.1485
REMARK 3 S31: -0.4185 S32: 0.1936 S33: 0.1467
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 38 E 77
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6930 6.2520 17.6960
REMARK 3 T TENSOR
REMARK 3 T11: -0.1432 T22: -0.1878
REMARK 3 T33: -0.1433 T12: 0.0082
REMARK 3 T13: 0.0011 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 2.5725 L22: 0.6656
REMARK 3 L33: 1.1175 L12: 0.2546
REMARK 3 L13: -0.5515 L23: 0.7099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0801 S12: 0.0428 S13: 0.0112
REMARK 3 S21: -0.0498 S22: -0.0133 S23: 0.0413
REMARK 3 S31: 0.2122 S32: -0.1104 S33: -0.0668
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 78 E 90
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0760 14.0600 13.0520
REMARK 3 T TENSOR
REMARK 3 T11: -0.1567 T22: -0.0916
REMARK 3 T33: -0.1486 T12: 0.0061
REMARK 3 T13: 0.0177 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.2076 L22: 0.7284
REMARK 3 L33: 0.3381 L12: -0.0040
REMARK 3 L13: -0.4963 L23: 0.3142
REMARK 3 S TENSOR
REMARK 3 S11: 0.1089 S12: 0.2699 S13: 0.1290
REMARK 3 S21: -0.1212 S22: 0.0247 S23: 0.1162
REMARK 3 S31: -0.1710 S32: -0.0272 S33: -0.1336
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 91 E 103
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0000 5.0930 25.4960
REMARK 3 T TENSOR
REMARK 3 T11: -0.1840 T22: -0.1338
REMARK 3 T33: -0.1734 T12: -0.0003
REMARK 3 T13: 0.0289 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 3.8968 L22: 3.7705
REMARK 3 L33: 13.0018 L12: -1.8323
REMARK 3 L13: 5.5464 L23: -4.0641
REMARK 3 S TENSOR
REMARK 3 S11: 0.1447 S12: 0.0210 S13: -0.1792
REMARK 3 S21: 0.0750 S22: -0.2054 S23: -0.1714
REMARK 3 S31: 0.3672 S32: 0.2714 S33: 0.0606
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 104 E 131
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5780 3.3330 14.1990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0712 T22: -0.0664
REMARK 3 T33: -0.1374 T12: 0.0534
REMARK 3 T13: 0.0240 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 3.9310 L22: 0.7856
REMARK 3 L33: 2.4758 L12: 0.3352
REMARK 3 L13: 2.3587 L23: -0.0941
REMARK 3 S TENSOR
REMARK 3 S11: 0.3455 S12: 0.5295 S13: -0.3321
REMARK 3 S21: -0.2466 S22: -0.2047 S23: 0.1203
REMARK 3 S31: 0.5719 S32: 0.3871 S33: -0.1408
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2Q5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : CHANNEL-CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16442
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.06500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1FM0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M SODIUM FORMATE, 0.1 M SODIUM
REMARK 280 ACETATE, PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 66.96100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.87700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.96100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.87700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTETRAMER GENERATED BY
REMARK 300 THE TWO FOLD AXIS.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 131.47377
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 41.70019
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN E 138
REMARK 465 LYS E 139
REMARK 465 GLY E 140
REMARK 465 ASN E 141
REMARK 465 TYR E 142
REMARK 465 GLU E 143
REMARK 465 GLU E 144
REMARK 465 ALA E 145
REMARK 465 LYS E 146
REMARK 465 ARG E 147
REMARK 465 GLU E 148
REMARK 465 GLU E 149
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH D 302 O HOH D 351 1.83
REMARK 500 O HOH E 179 O HOH E 242 2.00
REMARK 500 O HOH D 310 O HOH D 352 2.13
REMARK 500 O HOH D 313 O HOH D 353 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG E 107 O HOH E 236 2656 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER E 89 -0.45 71.98
REMARK 500 ALA D 7 -133.71 61.46
REMARK 500 SER D 75 34.19 -148.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NVI RELATED DB: PDB
REMARK 900 ORTHORHOMBIC CRYSTAL FORM OF E.COLI MOLYBDOPTERIN SYNTHASE
REMARK 900 RELATED ID: 1FM0 RELATED DB: PDB
REMARK 900 E.COLI MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)- ACTIVATED
REMARK 900 RELATED ID: 1FMA RELATED DB: PDB
REMARK 900 E.COLI MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)- COVALENT COMPLEX
REMARK 900 RELATED ID: 1NVJ RELATED DB: PDB
REMARK 900 DELETION MUTANT (DELTA 141) OF E.COLI MOLYBDOPTERIN SYNTHASE
DBREF 2Q5W E 2 149 UNP P65401 MOAE_STAAN 1 148
DBREF 2Q5W D 1 77 UNP Q5HDT7 Q5HDT7_STAAC 1 77
SEQADV 2Q5W HIS E 1 UNP P65401 EXPRESSION TAG
SEQRES 1 E 149 HIS MET LYS GLN PHE GLU ILE VAL ILE GLU PRO ILE GLN
SEQRES 2 E 149 THR GLU GLN TYR ARG GLU PHE THR ILE ASN GLU TYR GLN
SEQRES 3 E 149 GLY ALA VAL VAL VAL PHE THR GLY HIS VAL ARG GLU TRP
SEQRES 4 E 149 THR LYS GLY VAL LYS THR GLU TYR LEU GLU TYR GLU ALA
SEQRES 5 E 149 TYR ILE PRO MET ALA GLU LYS LYS LEU ALA GLN ILE GLY
SEQRES 6 E 149 ASP GLU ILE ASN GLU LYS TRP PRO GLY THR ILE THR SER
SEQRES 7 E 149 ILE VAL HIS ARG ILE GLY PRO LEU GLN ILE SER ASP ILE
SEQRES 8 E 149 ALA VAL LEU ILE ALA VAL SER SER PRO HIS ARG LYS ASP
SEQRES 9 E 149 ALA TYR ARG ALA ASN GLU TYR ALA ILE GLU ARG ILE LYS
SEQRES 10 E 149 GLU ILE VAL PRO ILE TRP LYS LYS GLU ILE TRP GLU ASP
SEQRES 11 E 149 GLY SER LYS TRP GLN GLY HIS GLN LYS GLY ASN TYR GLU
SEQRES 12 E 149 GLU ALA LYS ARG GLU GLU
SEQRES 1 D 77 MET LYS VAL LEU TYR PHE ALA GLU ILE LYS ASP ILE LEU
SEQRES 2 D 77 GLN LYS ALA GLN GLU ASP ILE VAL LEU GLU GLN ALA LEU
SEQRES 3 D 77 THR VAL GLN GLN PHE GLU ASP LEU LEU PHE GLU ARG TYR
SEQRES 4 D 77 PRO GLN ILE ASN ASN LYS LYS PHE GLN VAL ALA VAL ASN
SEQRES 5 D 77 GLU GLU PHE VAL GLN LYS SER ASP PHE ILE GLN PRO ASN
SEQRES 6 D 77 ASP THR VAL ALA LEU ILE PRO PRO VAL SER GLY GLY
HET GOL D 300 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *151(H2 O)
HELIX 1 1 THR E 14 ILE E 22 1 9
HELIX 2 2 TYR E 53 TRP E 72 1 20
HELIX 3 3 HIS E 101 VAL E 120 1 20
HELIX 4 4 PHE D 6 GLN D 14 1 9
HELIX 5 5 VAL D 28 TYR D 39 1 12
HELIX 6 6 GLN D 41 ASN D 43 5 3
SHEET 1 A 4 PHE E 5 VAL E 8 0
SHEET 2 A 4 ILE E 76 ARG E 82 1 O ILE E 79 N GLU E 6
SHEET 3 A 4 ILE E 91 SER E 99 -1 O ALA E 96 N SER E 78
SHEET 4 A 4 ALA E 28 HIS E 35 -1 N VAL E 30 O VAL E 97
SHEET 1 B 4 GLY E 84 LEU E 86 0
SHEET 2 B 4 THR E 45 ALA E 52 -1 N LEU E 48 O LEU E 86
SHEET 3 B 4 ILE E 122 TRP E 128 -1 O LYS E 125 N GLU E 49
SHEET 4 B 4 GLY E 131 TRP E 134 -1 O GLY E 131 N TRP E 128
SHEET 1 C 5 GLN D 17 ASP D 19 0
SHEET 2 C 5 LYS D 2 LEU D 4 -1 N VAL D 3 O GLU D 18
SHEET 3 C 5 THR D 67 ILE D 71 1 O VAL D 68 N LYS D 2
SHEET 4 C 5 GLN D 48 VAL D 51 -1 N GLN D 48 O ILE D 71
SHEET 5 C 5 GLU D 54 VAL D 56 -1 O GLU D 54 N VAL D 51
SHEET 1 D 2 LEU D 26 THR D 27 0
SHEET 2 D 2 PHE D 61 ILE D 62 -1 O ILE D 62 N LEU D 26
SITE 1 AC1 5 GLY D 77 GLY E 34 HIS E 35 LEU E 48
SITE 2 AC1 5 TYR E 50
CRYST1 133.922 45.754 41.772 90.00 93.36 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007467 0.000000 0.000438 0.00000
SCALE2 0.000000 0.021856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023981 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
